Binding and interactions of L-BABP to lipid membranes studied by molecular dynamic simulations

VILLARREAL MA, PERDUCA M, MONACO HL, MONTICH GG

Elsevier

Año: 2008 vol. 1778 p. 1390 - 1390

p class="MsoBodyText" style="MARGIN: 0cm 0cm 5.85pt">Chicken liver bile acid-binding protein (L-BABP) is a member of the fatty acid-binding proteins super family. The common fold is a b-barrel of ten strands capped with a short helix-loop-helix motif called portal region, which is involved in the uptake and release of non-polar ligands. Using multiple-run molecular dynamics simulations we studied the interactions of L-BABP with lipid membranes of anionic and zwitterionic phospholipids. The simulations were in agreement with our experimental observations regarding the electrostatic nature of the binding and the conformational changes of the protein in the membrane. We observed that L-BABP migrated from the initial position in the aqueous bulk ph